• anonymous
When a polypeptide is in its native conformation, there are weak interactions between its R groups. However, when it is denatured there are similar interactions between the protein groups and water. What then accounts for the greater stability of the native conformation?
  • Stacey Warren - Expert
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  • katieb
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  • aaronq
I guess it depends what the R groups are. I'm assuming they're non-polar since they have a greater stability in the proteins native conformation (which is likely a globular structure shielding the R groups from water).

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